Change of a conserved amino acid in the MYC2 and MYC3 transcription factors leads to release of JAZ repression and increased activity. Issue 4 (27th March 2015)
- Record Type:
- Journal Article
- Title:
- Change of a conserved amino acid in the MYC2 and MYC3 transcription factors leads to release of JAZ repression and increased activity. Issue 4 (27th March 2015)
- Main Title:
- Change of a conserved amino acid in the MYC2 and MYC3 transcription factors leads to release of JAZ repression and increased activity
- Authors:
- Goossens, Jonas
Swinnen, Gwen
Vanden Bossche, Robin
Pauwels, Laurens
Goossens, Alain - Abstract:
- <abstract abstract-type="main" id="nph13398-abs-0001"> <title>Summary</title> <p> <list id="nph13398-list-0001" list-type="bullet"> <list-item> <p>The bHLH transcription factor MYC2, together with its paralogues MYC3 and MYC4, is a master regulator of the response to the jasmonate (JA) hormone in Arabidopsis (<italic>Arabidopsis thaliana</italic>). In the absence of JA, JASMONATE ZIM (JAZ) proteins interact with the MYC proteins to block their activity. Understanding of the mechanism and specificity of this interaction is key to unravel JA signalling.</p> </list-item> <list-item> <p>We generated mutant MYC proteins and assessed their activity and the specificity of their interaction with the 12 Arabidopsis JAZ proteins.</p> </list-item> <list-item> <p>We show that the D94N mutation present in the <italic>atr2D</italic> allele of <italic>MYC3</italic> abolishes the interaction between MYC3 and most JAZ proteins. The same effect is observed when the corresponding conserved Asp (D105) was mutated in MYC2. Accordingly, MYC2<sup>D105N</sup> activated target genes in the presence of JAZ proteins, in contrast to wild‐type MYC2. JAZ1 and JAZ10 were the only JAZ proteins still showing interaction with the mutant MYC proteins, due to a second MYC interaction domain, besides the classical Jas domain.</p> </list-item> <list-item> <p>Our results visualize the divergence among JAZ proteins in their interaction with MYC proteins. Ultimately, the transferability of the Asp‐to‐Asn amino acid<abstract abstract-type="main" id="nph13398-abs-0001"> <title>Summary</title> <p> <list id="nph13398-list-0001" list-type="bullet"> <list-item> <p>The bHLH transcription factor MYC2, together with its paralogues MYC3 and MYC4, is a master regulator of the response to the jasmonate (JA) hormone in Arabidopsis (<italic>Arabidopsis thaliana</italic>). In the absence of JA, JASMONATE ZIM (JAZ) proteins interact with the MYC proteins to block their activity. Understanding of the mechanism and specificity of this interaction is key to unravel JA signalling.</p> </list-item> <list-item> <p>We generated mutant MYC proteins and assessed their activity and the specificity of their interaction with the 12 Arabidopsis JAZ proteins.</p> </list-item> <list-item> <p>We show that the D94N mutation present in the <italic>atr2D</italic> allele of <italic>MYC3</italic> abolishes the interaction between MYC3 and most JAZ proteins. The same effect is observed when the corresponding conserved Asp (D105) was mutated in MYC2. Accordingly, MYC2<sup>D105N</sup> activated target genes in the presence of JAZ proteins, in contrast to wild‐type MYC2. JAZ1 and JAZ10 were the only JAZ proteins still showing interaction with the mutant MYC proteins, due to a second MYC interaction domain, besides the classical Jas domain.</p> </list-item> <list-item> <p>Our results visualize the divergence among JAZ proteins in their interaction with MYC proteins. Ultimately, the transferability of the Asp‐to‐Asn amino acid change might facilitate the design of hyperactive transcription factors for plant engineering.</p> </list-item> </list> </p> </abstract> … (more)
- Is Part Of:
- New phytologist. Volume 206:Issue 4(2015)
- Journal:
- New phytologist
- Issue:
- Volume 206:Issue 4(2015)
- Issue Display:
- Volume 206, Issue 4 (2015)
- Year:
- 2015
- Volume:
- 206
- Issue:
- 4
- Issue Sort Value:
- 2015-0206-0004-0000
- Page Start:
- 1229
- Page End:
- 1237
- Publication Date:
- 2015-03-27
- Subjects:
- Botany -- Periodicals
580 - Journal URLs:
- http://nph.onlinelibrary.wiley.com/hub/journal/10.1111/(ISSN)1469-8137/ ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/nph.13398 ↗
- Languages:
- English
- ISSNs:
- 0028-646X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6085.000000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 4074.xml